J protein mutations and resulting proteostasis collapse.

Abstract:

:Despite a century of intensive investigation the effective treatment of protein aggregation diseases remains elusive. Ordinarily, molecular chaperones ensure that proteins maintain their functional conformation. The appearance of misfolded proteins that aggregate implies the collapse of the cellular chaperone quality control network. That said, the cellular chaperone network is extensive and functional information regarding the detailed action of specific chaperones is not yet available. J proteins (DnaJ/Hsp40) are a family of chaperone cofactors that harness Hsc70 (heat shock cognate protein of 70 kDa) for diverse conformational cellular tasks and, as such, represent novel clinically relevant targets for diseases resulting from the disruption of proteostasis. Here we review incisive reports identifying mutations in individual J protein chaperones and the proteostasis collapse that ensues.

journal_name

Front Cell Neurosci

authors

Koutras C,Braun JE

doi

10.3389/fncel.2014.00191

subject

Has Abstract

pub_date

2014-07-08 00:00:00

pages

191

issn

1662-5102

journal_volume

8

pub_type

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